Mouse PKM protein (Recombinant) (His-Tag) (STJP019335)

SPECIFICATIONS
HostE.coli
ImmunogenMouse
STJP019335
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General Information

Short DescriptionRecombinant-Mouse PKM-His-Tag protein was developed from e.coli and has a target region of His-Tag. For use in research applications.
ApplicationsSDS-PAGE/Enzyme Activity
HostE.coli
NoteSTRICTLY FOR FURTHER SCIENTIFIC RESEARCH USE ONLY (RUO). MUST NOT TO BE USED IN DIAGNOSTIC OR THERAPEUTIC APPLICATIONS.

Product Properties

Concentration0.5 mg/mL
FormulationLiquid in 20mM Tris-HCl buffer (pH8.5) containing 0.2M NaCl, 1mM DTT, 30% Glycerol
Storage InstructionFor short term storage, keep at +2C to +8C for up to 1 week. For long term storage, aliquot and store at-20C, and avoid repeat freeze-thaw cycles.
ImmunoreactivitySpecific activity: > 50, 000pmol/min/ug. One unit will convert 1.0pmole of phospho (enol) pyruvate to pyruvate per minute at pH 7.5 at 37C

Target Information

Gene SymbolPkm
Gene ID18746
Uniprot IDKPYM_MOUSE
Accession NumberNP_035229
ImmunogenMouse
Immunogen Region1-531aa
Immunogen SequenceMGSSHHHHHH SSGLVPRGSH MGSMPKPHSE AGTAFIQTQQ LHAAMADTFL EHMCRLDIDS APITARNTGI ICTIGPASRS VEMLKEMIKS GMNVARLNFS HGTHEYHAET IKNVREATES FASDPILYRP VAVALDTKGP EIRTGLIKGS GTAEVELKKG ATLKITLDNA YMEKCDENIL WLDYKNICKV VEVGSKIYVD DGLISLQVKE KGADFLVTEV ENGGSLGS

Additional Info

Tissue Specificity Embryonic stem cells and embryonal carcinoma cells.
Post Translational Modifications ISGylated. Under hypoxia, hydroxylated by EGLN3. Acetylation at Lys-305 is stimulated by high glucose concentration, it decreases enzyme activity and promotes its lysosomal-dependent degradation via chaperone-mediated autophagy. Isoform M2: Acetylated at Lys-433 by EP300, leading to impair phosphoenolpyruvate substrate-binding and promote its homodimerization and subsequent translocation to the nucleus. Deacetylation at Lys-433 by SIRT6 promotes its nuclear export into the cytoplasm, leading to suppress its nuclear localization and oncogenic function. Isoform M2: S-nitrosylation at Cys-423 and Cys-424 inhibits homotetramerization and pyruvate kinase activity. S-nitrosylation is indirectly inhibited by AKR1A1 which degrades S-nitroso-CoA, a cofactor required to S-nitrosylate proteins. FGFR1-dependent tyrosine phosphorylation is reduced by interaction with TRIM35.
Function Catalyzes the final rate-limiting step of glycolysis by mediating the transfer of a phosphoryl group from phosphoenolpyruvate (PEP) to ADP, generating ATP. The ratio between the highly active tetrameric form and nearly inactive dimeric form determines whether glucose carbons are channeled to biosynthetic processes or used for glycolytic ATP production. The transition between the 2 forms contributes to the control of glycolysis and is important for tumor cell proliferation and survival. Isoform M2: Isoform specifically expressed during embryogenesis that has low pyruvate kinase activity by itself and requires allosteric activation by D-fructose 1,6-bisphosphate (FBP) for pyruvate kinase activity. In addition to its pyruvate kinase activity in the cytoplasm, also acts as a regulator of transcription in the nucleus by acting as a protein kinase. Translocates into the nucleus in response to various signals, such as EGF receptor activation, and homodimerizes, leading to its conversion into a protein threonine- and tyrosine-protein kinase. Catalyzes phosphorylation of STAT3 at 'Tyr-705' and histone H3 at 'Thr-11' (H3T11ph), leading to activate transcription. Its ability to activate transcription plays a role in cancer cells by promoting cell proliferation and promote tumorigenesis. Promotes the expression of the immune checkpoint protein CD274 in BMAL1-deficient macrophages. May also act as a translation regulator for a subset of mRNAs, independently of its pyruvate kinase activity: associates with subpools of endoplasmic reticulum-associated ribosomes, binds directly to the mRNAs translated at the endoplasmic reticulum and promotes translation of these endoplasmic reticulum-destined mRNAs. Plays a role in caspase independent cell death of tumor cells. Isoform M1: Pyruvate kinase isoform expressed in adult tissues, which replaces isoform M2 after birth. In contrast to isoform M2, has high pyruvate kinase activity by itself and does not require allosteric activation by D-fructose 1,6-bisphosphate (FBP) for activity.
Protein Name Pyruvate Kinase Pkm
Pyruvate Kinase Muscle Isozyme
Threonine-Protein Kinase Pkm2
Tyrosine-Protein Kinase Pkm2
Database Links Reactome: R-MMU-6798695
Reactome: -MMU-70171
Reactome: -MMU-70268
Reactome: -MMU-9861718
Cellular Localisation Isoform M2: Cytoplasm
Nucleus
Translocates To The Nucleus In Response To Various Signals
Such As Egf Receptor Activation Or Apoptotic Stimuli
Nuclear Translocation Is Promoted By Acetylation By Ep300
Deacetylation By Sirt6 Promotes Its Nuclear Export In A Process Dependent Of Xpo4
Thereby Suppressing Its Ability To Activate Transcription And Promote Tumorigenesis
Isoform M1: Cytoplasm
Alternative Protein Names Pyruvate Kinase Pkm protein
Pyruvate Kinase Muscle Isozyme protein
Threonine-Protein Kinase Pkm2 protein
Tyrosine-Protein Kinase Pkm2 protein
Pkm protein
Pk3 protein
Pkm2 protein
Pykm protein

Information sourced from Uniprot.org

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